Header list of 1toz.pdb file
Complete list - v 10 2 Bytes
HEADER SIGNALING PROTEIN 15-JUN-04 1TOZ
TITLE NMR STRUCTURE OF THE HUMAN NOTCH-1 LIGAND BINDING REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NOTCH-1 EGF 11-13;
COMPND 5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS NOTCH, EGF, CALCIUM BINDING, LIGAND BINDING, MODULE, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.HAMBLETON,N.Y.VALEYEV,A.MURANYI,V.KNOTT,J.M.WERNER,A.J.MCMICHAEL,
AUTHOR 2 P.A.HANDFORD,A.K.DOWNING
REVDAT 4 10-NOV-21 1TOZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TOZ 1 VERSN
REVDAT 2 28-DEC-04 1TOZ 1 JRNL
REVDAT 1 12-OCT-04 1TOZ 0
JRNL AUTH S.HAMBLETON,N.V.VALEYEV,A.MURANYI,V.KNOTT,J.M.WERNER,
JRNL AUTH 2 A.J.MCMICHAEL,P.A.HANDFORD,A.K.DOWNING
JRNL TITL STRUCTURAL AND FUNCTIONAL PROPERTIES OF THE HUMAN NOTCH-1
JRNL TITL 2 LIGAND BINDING REGION
JRNL REF STRUCTURE V. 12 2173 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15576031
JRNL DOI 10.1016/J.STR.2004.09.012
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MURANYI,S.HAMBLETON,V.KNOTT,A.MCMICHAEL,P.A.HANDFORD,
REMARK 1 AUTH 2 A.K.DOWNING
REMARK 1 TITL 1H, 13C, AND 15N RESONANCE ASSIGNMENTS OF HUMAN NOTCH-1
REMARK 1 TITL 2 CALCIUM BINDING EGF DOMAINS 11-13
REMARK 1 REF J.BIOMOL.NMR V. 29 443 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15213460
REMARK 1 DOI 10.1023/B:JNMR.0000032521.42723.1A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.6, CYANA 1.0.6
REMARK 3 AUTHORS : GUNTERT, P. (CYANA), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INPUT MANUALLY ASSIGNED 15N-EDITED
REMARK 3 NOESY PEAKS, UNASSIGNED 13C-EDITED NOESY PEAKS. SEE PUBLICATION
REMARK 3 FOR FURTHER DETAILS.
REMARK 4
REMARK 4 1TOZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022805.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 15MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5-1MM PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : GE; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: ADDITIONAL TORSION ANGLE RESTRAINTS DERIVED USING TALOS.
REMARK 210 CALCIUM ATOMS INCORPORATED DURING STRUCTURE CALCULATIONS, AND
REMARK 210 RESTRAINTS INCORPORATED BASED ON THE CRYSTAL STRUCTURE 1EDM AS
REMARK 210 DESCRIBED.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H ILE A 430 O GLU A 437 1.43
REMARK 500 H THR A 445 O ILE A 451 1.47
REMARK 500 HD2 ASP A 464 O HIS A 486 1.53
REMARK 500 H ARG A 504 O GLU A 515 1.55
REMARK 500 O ASP A 414 H SER A 417 1.59
REMARK 500 O GLU A 455 HD21 ASN A 459 1.60
REMARK 500 N THR A 445 O ILE A 451 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LEU A 418 -92.94 -73.39
REMARK 500 1 GLU A 424 -106.94 68.61
REMARK 500 1 ALA A 426 90.04 168.08
REMARK 500 1 GLN A 442 -93.80 68.68
REMARK 500 1 THR A 445 -126.64 -101.93
REMARK 500 1 CYS A 449 62.87 87.61
REMARK 500 1 GLU A 450 15.04 -149.39
REMARK 500 1 ASN A 459 56.55 -144.28
REMARK 500 1 GLN A 462 -145.91 86.80
REMARK 500 1 ASP A 464 38.12 -151.19
REMARK 500 1 THR A 491 176.44 48.53
REMARK 500 1 GLU A 493 22.65 -146.20
REMARK 500 1 SER A 497 90.57 -166.50
REMARK 500 1 CYS A 499 -48.67 77.52
REMARK 500 1 LEU A 500 170.90 69.66
REMARK 500 1 HIS A 501 -110.96 67.39
REMARK 500 1 ASN A 510 -48.06 174.84
REMARK 500 1 PRO A 517 -162.95 -75.05
REMARK 500 1 THR A 518 -46.15 -168.28
REMARK 500 1 PHE A 520 -64.38 -95.95
REMARK 500 1 HIS A 523 -79.28 -115.15
REMARK 500 1 LEU A 524 -48.16 -171.55
REMARK 500 1 CYS A 525 97.49 63.97
REMARK 500 2 LEU A 418 -90.07 -73.03
REMARK 500 2 GLU A 424 -99.40 69.50
REMARK 500 2 ALA A 426 97.03 169.47
REMARK 500 2 GLN A 442 -100.01 65.49
REMARK 500 2 THR A 445 -123.90 -103.91
REMARK 500 2 CYS A 449 68.40 97.01
REMARK 500 2 GLU A 450 23.41 -161.42
REMARK 500 2 ASN A 459 51.49 -141.08
REMARK 500 2 GLN A 462 -150.20 86.06
REMARK 500 2 ALA A 465 125.93 -179.54
REMARK 500 2 CYS A 476 86.97 -154.86
REMARK 500 2 THR A 491 161.48 -40.67
REMARK 500 2 GLU A 493 25.34 -158.08
REMARK 500 2 SER A 497 70.68 159.62
REMARK 500 2 CYS A 499 103.13 -47.32
REMARK 500 2 LEU A 500 22.62 -141.64
REMARK 500 2 ASN A 510 -56.70 177.19
REMARK 500 2 GLU A 515 -163.29 -77.11
REMARK 500 2 PRO A 517 -162.31 -75.00
REMARK 500 2 THR A 518 -41.45 -165.92
REMARK 500 2 HIS A 523 72.35 -156.52
REMARK 500 2 CYS A 525 -71.65 -175.61
REMARK 500 3 LEU A 418 -78.22 -65.67
REMARK 500 3 CYS A 423 -19.76 -48.83
REMARK 500 3 GLU A 424 -100.95 69.15
REMARK 500 3 ALA A 426 94.64 -178.09
REMARK 500 3 GLN A 442 -98.86 52.15
REMARK 500
REMARK 500 THIS ENTRY HAS 425 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EMO RELATED DB: PDB
REMARK 900 STRUCTURE OF FIBRILLIN CALCIUM BINDING EGF DOMAINS 32-33
REMARK 900 RELATED ID: 1LMJ RELATED DB: PDB
REMARK 900 STRUCTURE OF FIBRILLIN CALCIUM BINDING EGF DOMAINS 12-13
REMARK 900 RELATED ID: 1HJ7 RELATED DB: PDB
REMARK 900 STRUCTURE OF LDL-RECEPTOR CALCIUM BINDING EGF DOMAINS A-B
DBREF 1TOZ A 411 526 UNP P46531 NOTC1_HUMAN 411 526
SEQADV 1TOZ ILE A 477 UNP P46531 MET 477 ENGINEERED MUTATION
SEQRES 1 A 116 GLN ASP VAL ASP GLU CYS SER LEU GLY ALA ASN PRO CYS
SEQRES 2 A 116 GLU HIS ALA GLY LYS CYS ILE ASN THR LEU GLY SER PHE
SEQRES 3 A 116 GLU CYS GLN CYS LEU GLN GLY TYR THR GLY PRO ARG CYS
SEQRES 4 A 116 GLU ILE ASP VAL ASN GLU CYS VAL SER ASN PRO CYS GLN
SEQRES 5 A 116 ASN ASP ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN
SEQRES 6 A 116 CYS ILE CYS MET PRO GLY TYR GLU GLY VAL HIS CYS GLU
SEQRES 7 A 116 VAL ASN THR ASP GLU CYS ALA SER SER PRO CYS LEU HIS
SEQRES 8 A 116 ASN GLY ARG CYS LEU ASP LYS ILE ASN GLU PHE GLN CYS
SEQRES 9 A 116 GLU CYS PRO THR GLY PHE THR GLY HIS LEU CYS GLN
HELIX 1 1 ASP A 414 GLY A 419 1 6
HELIX 2 2 GLU A 493 SER A 497 5 5
SHEET 1 A 2 GLY A 427 ASN A 431 0
SHEET 2 A 2 PHE A 436 CYS A 440 -1 O GLU A 437 N ILE A 430
SHEET 1 B 2 THR A 466 GLN A 470 0
SHEET 2 B 2 GLU A 473 ILE A 477 -1 O GLU A 473 N GLN A 470
SHEET 1 C 2 ARG A 504 ASP A 507 0
SHEET 2 C 2 PHE A 512 GLU A 515 -1 O GLU A 515 N ARG A 504
SSBOND 1 CYS A 416 CYS A 429 1555 1555 1.92
SSBOND 2 CYS A 423 CYS A 438 1555 1555 1.92
SSBOND 3 CYS A 440 CYS A 449 1555 1555 1.94
SSBOND 4 CYS A 456 CYS A 467 1555 1555 1.94
SSBOND 5 CYS A 461 CYS A 476 1555 1555 2.10
SSBOND 6 CYS A 478 CYS A 487 1555 1555 2.04
SSBOND 7 CYS A 494 CYS A 505 1555 1555 2.04
SSBOND 8 CYS A 499 CYS A 514 1555 1555 2.09
SSBOND 9 CYS A 516 CYS A 525 1555 1555 2.02
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - v 10 2 Bytes